The nuclear retention signal of HPV16 L2 protein is essential for incoming viral genome to transverse the trans-Golgi network

Virology. 2014 Jun:458-459:93-105. doi: 10.1016/j.virol.2014.04.024. Epub 2014 May 8.

Abstract

The Human papillomavirus (HPV) capsid is composed of the major and minor capsid proteins, L1 and L2, respectively. Infectious entry requires a complex series of conformational changes in both proteins that lead to uptake and allow uncoating to occur. During entry, the capsid is disassembled and host cyclophilins dissociate L1 protein from the L2/DNA complex. Herein, we describe a mutant HPV16 L2 protein (HPV16 L2-R302/5A) that traffics pseudogenome to the trans-Golgi network (TGN) but fails to egress. Our data provide further evidence that HPV16 traffics through the TGN and demonstrates that L2 is essential for TGN egress. Furthermore, we show that cyclophilin activity is required for the L2/DNA complex to be transported to the TGN which is accompanied by a reduced L1 protein levels.

Keywords: Cyclophilin; Entry; HPV; L1; L2; Trans-Golgi network.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Capsid Proteins / chemistry
  • Capsid Proteins / metabolism*
  • Genome, Viral*
  • HEK293 Cells
  • HeLa Cells
  • Human papillomavirus 16 / metabolism*
  • Humans
  • Mutation
  • Nuclear Localization Signals / metabolism*
  • Oncogene Proteins, Viral / chemistry
  • Oncogene Proteins, Viral / metabolism*
  • Protein Transport
  • Virus Internalization*
  • trans-Golgi Network / metabolism*

Substances

  • Capsid Proteins
  • L2 protein, Human papillomavirus type 16
  • Nuclear Localization Signals
  • Oncogene Proteins, Viral